Detail Information for IndEnz0002009537
IED ID IndEnz0002009537
Enzyme Type ID protease009537
Protein Name Capsid assembly scaffolding protein
Gene product O
GpO
Head morphogenesis protein
Scaffold protein

Cleaved into: Maturation protease
EC 3.4.21.-
Gene Name O
Organism Escherichia phage P2 (Bacteriophage P2)
Taxonomic Lineage Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Myoviridae (phages with contractile tails) Peduovirinae Peduovirus Escherichia phage P2 (Bacteriophage P2)
Enzyme Sequence MAKKVSKFFRIGVEGDTCDGRVISAQDIQEMAETFDPRVYGCRINLEHLRGILPDGIFKRYGDVAELKAEKIDDDSALKGKWALFAKITPTDDLIAMNKAAQKVYTSMEIQPNFANTGKCYLVGLAVTDDPASLGTEYLEFCRTAKHNPLNRFKLSPENLISVATPVELEFEDLPETVFTALTEKVKSIFGRKQASDDARLNDVHEAVTAVAEHVQEKLSATEQRLAEMETAFSALKQEVTDRADETSQAFTRLKNSLDHTESLTQQRRSKATGGGGDALMTNC
Enzyme Length 284
Uniprot Accession Number P25478
Absorption
Active Site ACT_SITE 19; /evidence=ECO:0000269|PubMed:19064277; ACT_SITE 48; /evidence=ECO:0000269|PubMed:19064277; ACT_SITE 107; /evidence=ECO:0000269|PubMed:19064277
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Scaffolding protein and protease involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are cleaved by the viral protease activity. {ECO:0000305|PubMed:19064277}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (2); Coiled coil (1); Compositional bias (1); Region (1); Site (1)
Keywords Coiled coil;Hydrolase;Protease;Reference proteome;Serine protease;Viral capsid assembly;Viral capsid maturation;Viral release from host cell
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Autocleaves itself into an N-terminal fragment containing the protease activity, that remains in the capsid following maturation. {ECO:0000269|PubMed:17931675}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 31,446
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda